OFUT2_CAEEL
ID OFUT2_CAEEL Reviewed; 424 AA.
AC Q8WR51;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2;
DE EC=2.4.1.221 {ECO:0000269|PubMed:26854667};
DE AltName: Full=Patterning defective protein 2;
DE AltName: Full=Peptide-O-fucosyltransferase 2;
DE Short=O-FucT-2;
DE Flags: Precursor;
GN Name=pad-2; ORFNames=K10G9.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAL65193.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15233996; DOI=10.1016/j.ygeno.2004.04.002;
RA Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F.,
RA Antonarakis S.E., Guipponi M.;
RT "The Caenorhabditis elegans ortholog of C21orf80, a potential new protein
RT O-fucosyltransferase, is required for normal development.";
RL Genomics 84:320-330(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4] {ECO:0007744|PDB:5FOE}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF MUTANT LYS-298 AND LYS-299 IN
RP COMPLEX WITH GDP AND HUMAN TSR1 TSR DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, GLYCOSYLATION AT ASN-205, AND DISULFIDE BONDS.
RX PubMed=26854667; DOI=10.1038/nchembio.2019;
RA Valero-Gonzalez J., Leonhard-Melief C., Lira-Navarrete E., Jimenez-Oses G.,
RA Hernandez-Ruiz C., Pallares M.C., Yruela I., Vasudevan D., Lostao A.,
RA Corzana F., Takeuchi H., Haltiwanger R.S., Hurtado-Guerrero R.;
RT "A proactive role of water molecules in acceptor recognition by protein O-
RT fucosyltransferase 2.";
RL Nat. Chem. Biol. 12:240-246(2016).
CC -!- FUNCTION: Catalyzes the reaction that attaches fucose through an O-
CC glycosidic linkage to a conserved serine or threonine residue in the
CC consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats
CC (TSRs) where C1 and C2 are the first and second cysteines of the
CC repeat, respectively (PubMed:15233996, PubMed:26854667). O-fucosylates
CC members of several protein families including the ADAMTS superfamily
CC and the thrombospondin (TSP) and spondin families (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2G5, ECO:0000269|PubMed:15233996,
CC ECO:0000269|PubMed:26854667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-
CC L-seryl-[protein] + GDP + H(+); Xref=Rhea:RHEA:63644, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:17914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189632; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:26854667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:26854667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-
CC fucosyl)-L-threonyl-[protein] + GDP + H(+); Xref=Rhea:RHEA:70491,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:17915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189631; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:26854667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:26854667};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:26854667}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y2G5}. Golgi apparatus
CC {ECO:0000269|PubMed:15233996}. Note=Mainly located in the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:Q9Y2G5}.
CC -!- TISSUE SPECIFICITY: Expressed in the anterior part of embryos, in the
CC hypodermal and neuronal cells of the head. Expressed at different
CC levels in a variety of cell types after hatching, including neuronal,
CC hypodermal, muscle, intestinal, and somatic gonadal cells. Expressed in
CC the nerve ring around the pharynx, in dorsal and ventral nerve cords,
CC intestine, and a variety of hypodermal cells of L1-L3 larvae. Expressed
CC in gonadal sheath cells, spermatheca, and tissues surrounding the vulva
CC of adult hermaphrodites, and in the body wall muscle and hypodermal
CC cells of adults of both sexes. {ECO:0000269|PubMed:15233996}.
CC -!- DEVELOPMENTAL STAGE: Expressed starts at morphogenetic embryonic stages
CC and continues throughout development. {ECO:0000269|PubMed:15233996}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
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DR EMBL; AF455271; AAL65193.1; -; mRNA.
DR EMBL; Z36282; CAD45602.1; -; Genomic_DNA.
DR RefSeq; NP_001255070.1; NM_001268141.1.
DR PDB; 5FOE; X-ray; 1.98 A; A/B=1-424.
DR PDBsum; 5FOE; -.
DR AlphaFoldDB; Q8WR51; -.
DR SMR; Q8WR51; -.
DR STRING; 6239.K10G9.3b; -.
DR CAZy; GT68; Glycosyltransferase Family 68.
DR iPTMnet; Q8WR51; -.
DR EPD; Q8WR51; -.
DR PaxDb; Q8WR51; -.
DR EnsemblMetazoa; K10G9.3a.1; K10G9.3a.1; WBGene00010757.
DR GeneID; 259529; -.
DR UCSC; K10G9.3; c. elegans.
DR CTD; 259529; -.
DR WormBase; K10G9.3a; CE31715; WBGene00010757; pad-2.
DR eggNOG; ENOG502QPS6; Eukaryota.
DR GeneTree; ENSGT00390000007989; -.
DR InParanoid; Q8WR51; -.
DR PhylomeDB; Q8WR51; -.
DR BRENDA; 2.4.1.221; 1045.
DR Reactome; R-CEL-5173214; O-glycosylation of TSR domain-containing proteins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8WR51; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010757; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; Q8WR51; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0036066; P:protein O-linked fucosylation; IDA:UniProtKB.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; PTHR13398; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond;
KW Endoplasmic reticulum; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..424
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /id="PRO_0000012157"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 51..55
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT BINDING 288..290
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT BINDING 366
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT BINDING 383..384
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT SITE 391
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667,
FT ECO:0000269|PubMed:26854667"
FT DISULFID 154..187
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT DISULFID 407..414
FT /evidence="ECO:0000269|PubMed:26854667,
FT ECO:0007744|PDB:5FOE"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 54..73
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:5FOE"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:5FOE"
SQ SEQUENCE 424 AA; 50106 MW; 2A35F5FC04EF70B3 CRC64;
MHFFPIQLLV LFFAEKIAFA ENSDQTVSRV DSNRYSVAAE KKFLLYDVNF GEGFNLRRDV
YMRVANTVRS LRDSGENYIL VLPPWGRLHH WKRMEVALSW RLFFDLESLN RFIPVIEFED
FLDENRPIDQ VIYLQHYAEG WGTEYVRKFE KRSCLPPAES HYKQVEEFKW KGWFYSYEDV
YSRNFQCVSI QGDSGTLKDL LKHSNFSEST SIMVDRAETI LHEHYGEVDY WKARRSMRYS
NDLVDVADAF RKKYLDSDDK RDKTKLVDDW TKEKPRRTAI GGPYLGIHWR RRDFLYARRA
QLPTIPGTAK ILQDLCKKLD LQKIYLATDA PDQEVDELKA LLNGELEVYR FTDTQKLNDG
QIAIIDQYLC AHAAYFIGSY ESTFTFRIQE DREIIGFPIS TTFNRLCPDT EPTCEQPAKW
KIVY
